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Links from Protein

Items: 10

1.

multicopper oxidase domain-containing protein

This entry contains many divergent copper oxidase-like domains that are not recognised by the Pfam:PF00394 model. [1]. 2404764. The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin.. Modelling and structural relationships.. Messerschmidt A, Huber R;. Eur J Biochem 1990;187:341-352.. [2]. 1548698. Refined crystal structure of ascorbate oxidase at 1.9 A. resolution.. Messerschmidt A, Ladenstein R, Huber R, Bolognesi M, Avigliano. L, Petruzzelli R, Rossi A, Finazzi-Agro A;. J Mol Biol 1992;224:179-205.. [3]. 10573417. Natural engineering principles of electron tunnelling in. biological oxidation-reduction.. Page CC, Moser CC, Chen X, Dutton PL;. Nature 1999;402:47-52.. [4]. 7599131. X-ray absorption studies and homology modeling define the. structural features that specify the nature of the copper site. in rusticyanin.. Grossmann JG, Ingledew WJ, Harvey I, Strange RW, Hasnain SS;. Biochemistry 1995;34:8406-8414. (from Pfam)

GO Terms:
Molecular Function:
copper ion binding (GO:0005507)
Date:
2024-08-14
Family Accession:
NF019352.5
Method:
HMM
2.

multicopper oxidase domain-containing protein

This entry contains many divergent copper oxidase-like domains that are not recognised by the Pfam:PF00394 model. [1]. 2404764. The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin.. Modelling and structural relationships.. Messerschmidt A, Huber R;. Eur J Biochem 1990;187:341-352.. [2]. 1548698. Refined crystal structure of ascorbate oxidase at 1.9 A. resolution.. Messerschmidt A, Ladenstein R, Huber R, Bolognesi M, Avigliano. L, Petruzzelli R, Rossi A, Finazzi-Agro A;. J Mol Biol 1992;224:179-205.. [3]. 10573417. Natural engineering principles of electron tunnelling in. biological oxidation-reduction.. Page CC, Moser CC, Chen X, Dutton PL;. Nature 1999;402:47-52.. [4]. 7599131. X-ray absorption studies and homology modeling define the. structural features that specify the nature of the copper site. in rusticyanin.. Grossmann JG, Ingledew WJ, Harvey I, Strange RW, Hasnain SS;. Biochemistry 1995;34:8406-8414. (from Pfam)

GO Terms:
Molecular Function:
copper ion binding (GO:0005507)
Molecular Function:
oxidoreductase activity (GO:0016491)
Date:
2024-08-14
Family Accession:
NF019351.5
Method:
HMM
3.

Multicopper oxidase

Many of the proteins in this family contain multiple similar copies of this plastocyanin-like domain. [1]. 2404764. The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin.. Modelling and structural relationships.. Messerschmidt A, Huber R;. Eur J Biochem 1990;187:341-352.. [2]. 1548698. Refined crystal structure of ascorbate oxidase at 1.9 A. resolution.. Messerschmidt A, Ladenstein R, Huber R, Bolognesi M, Avigliano. L, Petruzzelli R, Rossi A, Finazzi-Agro A;. J Mol Biol 1992;224:179-205. (from Pfam)

Date:
2024-08-14
Family Accession:
NF012612.5
Method:
HMM
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.
new record, indexing in progress
Family Accession:
8.
new record, indexing in progress
Family Accession:
9.
new record, indexing in progress
Family Accession:
10.

copper resistance system multicopper oxidase

This HMM represents the CopA copper resistance protein family. CopA is related to laccase (benzenediol:oxygen oxidoreductase) and L-ascorbate oxidase, both copper-containing enzymes. Most members have a typical TAT (twin-arginine translocation) signal sequence with an Arg-Arg pair. Twin-arginine translocation is observed for a large number of periplasmic proteins that cross the inner membrane with metal-containing cofactors already bound. The combination of copper-binding sites and TAT translocation motif suggests a mechansism of resistance by packaging and export.

GO Terms:
Molecular Function:
copper ion transmembrane transporter activity (GO:0005375)
Molecular Function:
copper ion binding (GO:0005507)
Biological Process:
copper ion transport (GO:0006825)
Cellular Component:
periplasmic space (GO:0042597)
Date:
2024-06-21
Family Accession:
TIGR01480.1
Method:
HMM
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